Study of human, rabbit and pig oxyhemoglobins using high velocity resolution Mössbauer spectroscopy in relation to their structural and functional variations / Oshtrakh M.I., Kumar A., Kundu S., Berkovsky A.L., Semionkin V.A. // Journal of Molecular Structure. - 2011. - V. 993, l. 1-3. - P. 292-296.

ISSN:

00222860

Type:

Conference Paper

Abstract:

Normal human adult, rabbit and pig oxyhemoglobins in frozen red blood cell solutions were studied using Mössbauer spectroscopy with a high velocity resolution. Spectra were analyzed using two models with and without accounting for the heme iron electronic structure non-equivalence in α- and β-subunits of tetrameric hemoglobins. The observed differences of Mössbauer hyperfine parameters were related to structural variations in human, rabbit and pig oxyhemoglobins as well as to the differences in ligand binding affinities of these proteins. © 2010 Elsevier B.V. All rights reserved.

Author keywords:

Heme iron structure; Human adult; Hyperfine parameters; Mössbauer spectroscopy with a high velocity resolution; Rabbit and pig oxyhemoglobins

Index keywords:

Heme iron; Human adult; Hyperfine parameters; Rabbit and pig oxyhemoglobins; Ssbauer spectroscopies; Binding energy; Blood; Electronic structure; Hemoglobin; Iron; Mammals; Porphyrins; Velocity; Pig i

DOI:

10.1016/j.molstruc.2010.11.035

Смотреть в Scopus:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-79955473405&doi=10.1016%2fj.molstruc.2010.11.035&partnerID=40&md5=56f9f509ace6433ae38b3e67de742f7d

Соавторы в МНС:

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Поле	Значение
Link	https://www.scopus.com/inward/record.uri?eid=2-s2.0-79955473405&doi=10.1016%2fj.molstruc.2010.11.035&partnerID=40&md5=56f9f509ace6433ae38b3e67de742f7d
Affiliations	Faculty of Physical Techniques and Devices for Quality Control, Ural Federal University, 620002 Ekaterinburg, Russian Federation; Department of Biochemistry, University of Delhi South Campus, Benito Juarez Road, New Delhi 110 021, India; Hematological Research Center, Russian Academy of Medical Sciences, 125167 Moscow, Russian Federation; Faculty of Experimental Physics, Ural Federal University, 620002 Ekaterinburg, Russian Federation
Author Keywords	Heme iron structure; Human adult; Hyperfine parameters; Mössbauer spectroscopy with a high velocity resolution; Rabbit and pig oxyhemoglobins
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Correspondence Address	Oshtrakh, M. I.; Faculty of Physical Techniques and Devices for Quality Control, Ural Federal University, 620002 Ekaterinburg, Russian Federation; email: oshtrakh@mail.utnet.ru
CODEN	JMOSB
Language of Original Document	English
Abbreviated Source Title	J. Mol. Struct.
Source	Scopus